Abstract
Polymeric β-chitosan allomorph characterized by parallel arrangement of linear polysaccharide comprised of β-(1 → 4)-linked-D-glucosamine and N-acetyl-D-glucosamine was isolated and characterized from the gladius of Indian Ocean Squid (Uroteuthis duvaucelii) and spineless cuttlefish (Sepiella inermis). The β-chitosan from U. duvaucelii displayed considerably greater attenuation potential against hydroxymethylglutaryl coenzyme-A reductase, dipeptidyl peptidase-4, I converting enzyme, and 5-lipoxygenase (IC50 0.15–0.53 mg mL−1) than those exhibited by α-chitosan of comparable molecular weight. Comparatively lesser conformational rigidity of β-chitin could result in its greater susceptibility to deacetylation (86–87%) contrasted to the α-allomorph (~83%), consequently delivering enhanced functionalities than those exhibited by α-chitosan. Porous β-chitosan scaffolds displayed an average pore size of lesser than 50 μm, and its binding capacity was significantly higher than that exhibited by α-chitosan (p < 0.05). Potential pharmacological activities reinforced by lesser binding affinities and intermolecular energy of β-chitosan with the target enzymes recognized its prospective biomedical applications.
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